User:Daniel Seeman/Alpha-1-antitrypsin

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{{STRUCTURE_1atu | PDB=1atu | SCENE= }}
{{STRUCTURE_1atu | PDB=1atu | SCENE= }}
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'''Alpha-1-antitrypsin''' (or α1-antitrypsin, A1AT) is an inhibitor of trypsin. It is a member of the Serine Protease Inhibitor ([[:Category:Serpin|Serpin]]) family, and as such undergoes a conformational change where a loop region becomes ordered as a Beta Strand. In this case trypsin is inhibited when a covalent bond is formed to A1AT.
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'''Alpha-1-antitrypsin''' (or α1-antitrypsin, A1AT) is an inhibitor of Trypsin. It is a member of the Serine Protease Inhibitor ([[:Category:Serpin|Serpin]]) family, and as such undergoes a conformational change where a loop region becomes ordered as a Beta Strand. In this case Trypsin is inhibited when a covalent bond is formed to A1AT.
=== See Also ===
=== See Also ===

Revision as of 15:17, 25 November 2008

PDB ID 1atu

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1atu, resolution 2.70Å ()
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Alpha-1-antitrypsin (or α1-antitrypsin, A1AT) is an inhibitor of Trypsin. It is a member of the Serine Protease Inhibitor (Serpin) family, and as such undergoes a conformational change where a loop region becomes ordered as a Beta Strand. In this case Trypsin is inhibited when a covalent bond is formed to A1AT.

See Also

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Daniel Seeman

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